|JKMRS Volume 25, No 1, pp 8, Backbone NMR chemical shift assig...|
|2021년 03월 20일 / 조회수: 185|
Bokyung Kim and Jin Hae Kim*
Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology, Daegu 42988, Republic of Korea
Received Mar 19, 2021; Revised Mar 19, 2021; Accepted Mar 19, 2021
Abstract Transthyretin (TTR) is an important transporter protein for thyroxine (T4) and a holo-retinol protein in human. In its native state, TTR forms a tetrameric complex to construct the hydrophobic binding pocket for T4. On the other hand, this protein is also infamous for its amyloidogenic propensity, which causes various human diseases, such as senile systemic amyloidosis and familial amyloid polyneuropathy/cardiomyopathy. In this work, to investigate various structural features of TTR with solution-state nuclear magnetic resonance (NMR) spectroscopy, we conducted backbone NMR signal assignments. Except the N-terminal two residues and prolines, backbone 1H-15N signals of all residues were successfully assigned with additional chemical shift information of 13CO, 13Cα, and 13Cβ for most residues. The chemical shift information reported here will become an important basis for subsequent structural and functional studies of TTR.
Keywords transthyretin, transthyretin amyloidosis, NMR spectroscopy, chemical shift assignment